Resonance assignment of proteins with high shift degeneracy based on 5D spectral information encoded in G2FT NMR experiments.

Resonance assignment of proteins with high shift degeneracy based on 5D spectral information encoded in G2FT NMR experiments. Research Abstract Details 

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Resonance assignment of proteins with high shift degeneracy based on 5D spectral information encoded in G2FT NMR experiments. Abstract Text:

Hanudatta S Atreya,Alexander Eletsky,Thomas Szyperski,

A suite of novel (5,3)D G2FT triple resonance NMR experiments encoding highly resolved 5D spectral information is presented for sequential resonance assignment of proteins exhibiting high chemical shift degeneracy. Efficient resonance assignment is achieved by separate joint sampling of (i) chemical shifts which solely serve to provide increased resolution and (ii) shifts which also provide sequential connectivities. In these G2FT experiments, two G-matrix transformations are employed. Peaks are resolved along a first GFT dimension at both Omega(15N) + Omega(13C') and Omega(15N) - Omega(13C'), or at Omega(15N) + Omega(13Calpha) and Omega(15N) - Omega(13Calpha), to break backbone 15N,1HN chemical shift degeneracy. Sequential connectivities are established along a second GFT dimension by measuring intraresidue and sequential correlations at 2Omega(13Calpha), Omega(13Calpha + 13Cbeta), and Omega(13Calpha - 13Cbeta), or at Omega(13Calpha + 1Halpha) and Omega(13Calpha - 1Halpha), to resolve 13Calpha/beta,1Halpha chemical shift degeneracy. It is demonstrated that longitudinal proton relaxation optimization of out-and-back implementations suitable for deuterated proteins and nonlinear data sampling combined with maximum entropy reconstruction further accelerate G2FT NMR data acquisition speed. As a result, the spectral information can be obtained within hours, so that (5,3)D G2FT experiments are viable options for high-throughput structure determination in structural genomics. Applications are presented for 17 kDa alpha-helical protein YqbG and 13.5 kDa protein rps24e, targets of the Northeast Structural Genomics consortium, as well as for 9 kDa protein Z-domain. The high resolving power of the G2FT NMR experiments makes them attractive choices to study alpha-helical globular/membrane or (partially) unfolded proteins, thus promising to pave the way for NMR-based structural genomics of membrane proteins.

Resonance assignment of proteins with high shift degeneracy based on 5D spectral information encoded in G2FT NMR experiments. Publishing Authors By Initials

HS Atreya,A Eletsky,T Szyperski,

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Resonance assignment of proteins with high shift degeneracy based on 5D spectral information encoded in G2FT NMR experiments. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Journal of the American Chemical Society

VOLUME: 127

Page Numbers: 4554-5

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 6

MONTH: Apr

YEAR: 2005

Resonance assignment of proteins with high shift degeneracy based on 5D spectral information encoded in G2FT NMR experiments. Information

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LANGUAGE: eng

NlmUniqueID: 7503056

Resonance assignment of proteins with high shift degeneracy based on 5D spectral information encoded in G2FT NMR experiments. Keywords Mesh Terms:

KEYWORDS: Proteins

MESH TERMS: chemistry

Chemical & Substance for Abstract: Resonance assignment of proteins with high shift degeneracy based on 5D spectral information encoded in G2FT NMR experiments. Information

Substance Name: Proteins

Registry Number: 0

Grant and Affiliation Information for Resonance assignment of proteins with high shift degeneracy based on 5D spectral information encoded in G2FT NMR experiments.

AFFILIATION: Department of Chemistry, State University of New York at Buffalo, Buffalo, NY 14260, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: P50 GM 62413-01

ACRONYM: GM

MEDLINETA: J Am Chem Soc

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